SPR-technology enables the interaction between biomolecules to be monitored in real time using label-free assay formats. The underlying physics of the principles of SPR are complicated.
However, a working knowledge of the technique doesn't require a detailed understanding of the physics. In brief, SPR-instruments visualize the progress of biomolecular binding through time by detecting the change in mass concentration that occurs on a sensor chip surface during the binding and the dissociation processes.
One of the interacting molecules is immobilized on the sensor surface. The other molecule (the analyte) is then injected in solution over the sensor surface. As analytes from the injected sample bind to the interacting partner immobilized on the sensor surface, the change in mass at the surface is detected and plotted against time as a sensorgram. SPR-biosensors provide information on affinity, binding kinetics (association, dissociation rates) and transition state thermodynamic of an interaction, and can also be used in concentration analyses.
We are active in developing applications for food analysis e.g:
Interaction between folates and bovine folate binding protein (FBP)
Interaction between vitamin D and Vitamin-D binding protein (VDBP)
Concentration analysis fo acute phase protine (koptoglobin)
Analysis of antimicrobial drug residues
Active researchers:
Linnéa Nygren-Babol, PhD
Åse Sternesjö, Professor
Maria Åkerstedt, AgrDr